http://purl.uniprot.org/citations/35650207 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/35650207 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein degradation, a major eukaryotic response to cellular signals, is subject to numerous layers of regulation. In yeast, the evolutionarily conserved GID E3 ligase mediates glucose-induced degradation of fructose-1,6-bisphosphatase (Fbp1), malate dehydrogenase (Mdh2), and other gluconeogenic enzymes. "GID" is a collection of E3 ligase complexes; a core scaffold, RING-type catalytic core, and a supramolecular assembly module together with interchangeable substrate receptors select targets for ubiquitylation. However, knowledge of additional cellular factors directly regulating GID-type E3s remains rudimentary. Here, we structurally and biochemically characterize Gid12 as a modulator of the GID E3 ligase complex. Our collection of cryo-EM reconstructions shows that Gid12 forms an extensive interface sealing the substrate receptor Gid4 onto the scaffold, and remodeling the degron binding site. Gid12 also sterically blocks a recruited Fbp1 or Mdh2 from the ubiquitylation active sites. Our analysis of the role of Gid12 establishes principles that may more generally underlie E3 ligase regulation."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-022-30803-9"xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Cheng J."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Mann M."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Schulman B.A."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Qiao S."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Lee C.W."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Karayel O."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Steigenberger B."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Vu D.T."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "von Gronau S."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Chrustowicz J."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Wilfling F."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Sherpa D."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/author | "Duennebacke M."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/date | "2022"xsd:gYear |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/name | "Nat Commun"xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/pages | "3041"xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/title | "Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation."xsd:string |
http://purl.uniprot.org/citations/35650207 | http://purl.uniprot.org/core/volume | "13"xsd:string |
http://purl.uniprot.org/citations/35650207 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/35650207 |
http://purl.uniprot.org/citations/35650207 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/35650207 |
http://purl.uniprot.org/uniprot/#_P40208-mappedCitation-35650207 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/35650207 |
http://purl.uniprot.org/uniprot/#_P38263-mappedCitation-35650207 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/35650207 |